either NAD+ or NADP+ serve as coenzyme. Double-reciprocal plots of activity versus pyridine nucleotide concentration are biphasic. The Km values for NADP+ are lower but a higher Vmax is observed with NAD+

either NAD+ or NADP+ serve as coenzyme. Double-reciprocal plots of activity versus pyridine nucleotide concentration are biphasic. The Km values for NADP+ are lower but a higher Vmax is observed with NAD+

either NAD+ or NADP+ serve as coenzyme. Double-reciprocal plots of activity versus pyridine nucleotide concentration are biphasic. The Km values for NADP+ are lower but a higher Vmax is observed with NAD+

either NAD+ or NADP+ serve as coenzyme. Double-reciprocal plots of activity versus pyridine nucleotide concentration are biphasic. The Km values for NADP+ are lower but a higher Vmax is observed with NAD+

addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme

addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme

addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme

addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme

the lactams of DL-erythro-3,5-diaminohexanoate and DL-threo-3,5-diaminohexanoatae and 2-methylpyrrolidone-5-carboxylic acid have no effect on activity. Acetate (10 mM), butyrate (10 mM), acetyl phosphate (2 mM), or acetyl-CoA (0.62 mM) have no effect on enzyme activity